Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 474, Issue 1, Pages 51-56Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.04.058
Keywords
Protein neddylation; Protein ubiquitination; Nedd8; Ubiquitin ligase; Smurf2
Categories
Funding
- Chinese National Natural Science Foundation [31471326, 31470035]
- Beijing Natural Science Foundation [49714285]
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E3 ubiquitin ligases are pivotal effectors of the ubiquitin-proteasome system as they determine the substrate specificity and transfer ubiquitin to the substrate. HECT-type ubiquitin ligase Smad ubiquitination regulatory factor 2 (Smurf2) has been demonstrated functions as a tumor suppressor. However, the mechanisms underlying regulation of Smurf2 is still unclear. Here we show that ubiquitin-like protein Nedd8 targets the HECT-type ubiquitin ligase Smurf2 for neddylation, and promotes Smurf2 degradation. Neddylation of Smurf1 activates its ubiquitin ligase activity and Smurf2 exerts Nedd8 ligase activity. This study provided new clues of Smurf2 activation regulation. (C) 2016 Elsevier Inc. All rights reserved.
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